Cholera Toxin B subunit; CTxB; Cholera Toxin B; CTB
Purity
>95%
Format
Liquid
Preservative
None
Storage
Store at -20 °C for one year.
Introduction
Cholera toxin belongs to the AB5 –subunit family oftoxins.The native hexameric protein has a molecular mass of ~85 kDa and contains two subunits. It consists of a single A subunit (~27.2 kDa), responsible for the ADP-ribosylation activity, and five B subunits(~11.6 kDa each), which are arranged as a pentameric ring with an apparent 5-fold symmetry and are associated with the cell surface receptor binding and subsequent internalization (transmembrane transport)of the enzymatic component.
Keywords
Cholera Toxin B subunit; CTxB; Cholera Toxin B; CTB
Citations
Publication ()
Have you cited DAGC751 in a publication? Let us know and earn a reward for your research.
Background
Cholera toxin is a potent enterotoxin from Vibrio cholerae with specific structural and functional features. It consists of an A subunit (CTA) and five B subunits (CTB), making it a molecular meshwork. The CTA is the toxic unit, while CTB is the non-toxic receptor-binding unit capable of attaching to GM1 receptors on cell membranes. This binding allows antigens linked to the B subunit to maintain prolonged contact with immune cells, inducing oral tolerance to ingested antigens. CT is extremely toxic, with as little as 8μg capable of causing severe diarrhea. However, it simultaneously exhibits strong immunogenicity, making it an important mucosal immune adjuvant.
Figure 1. Structure of cholera toxin (Source: Day CA, et al. 2015)
Despite CT's potent immunogenicity and adjuvant effects, its high toxicity precludes direct human application. To address this issue, researchers have developed various improvement strategies. The primary approach involves using genetic engineering to modify the A subunit or utilizing the CTB alone as an adjuvant. As a non-toxic mucosal carrier molecule, CTB shows promising applications in vaccine development and immunotherapy. It can form new antigen complexes with other antigens through chemical conjugation or genetic fusion. This method not only induces oral tolerance but also significantly reduces the required antigen dose. In practical applications, CTB has been proven to effectively enhance immune responses, particularly in inducing mucosal immunity and oral tolerance. For instance, in peanut allergy research, mixtures of CTB and peanut antigens significantly increased levels of specific immunoregulatory cells and cytokines, offering new insights into allergy treatment. Overall, while CT itself cannot be directly applied to humans due to toxicity issues, its B subunit CTB has become an important tool in vaccine development and immunotherapy, especially in inducing mucosal immunity and oral tolerance. As research progresses, CTB's potential applications in immunology are expected to expand further.
Beyond its applications in vaccines and immunomodulation, CTB demonstrates potential in other areas. In certain autoimmune disease models, CTB exhibits anti-inflammatory properties. Its potential to induce oral tolerance, suppress allergies, and mitigate autoimmune diseases has attracted researchers' attention. Additionally, CTB serves as a research tool, such as a neuronal tracer for mapping neural pathways and for identifying lipid raft structures on cell surfaces.
Alternative Names
Recombinant CTB subunit [FITC]
References
1. Day CA, et al. Functions of cholera toxin B-subunit as a raft cross-linker. Essays Biochem. 2015;57:135-45.
2. Stratmann T. Cholera Toxin Subunit B as Adjuvant--An Accelerator in Protective Immunity and a Break in Autoimmunity. Vaccines (Basel). 2015 Jul 24;3(3):579-96.
My Review for Recombinant Cholera Toxin B subunit [FITC]
Creative Diagnostics products are for RESEARCH USE ONLY, please make sure your review is research based.
Required fields are marked with *
Terms and conditions:
We will select high-quality review customers and offer a $30 coupon for your next purchase.
All product reviews must be submitted in the English language.
Creative Diagnostics will not share any personal information of applicants, and all information will be treated with strict confidentiality and will not be sold or disclosed to a third party.